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3.5.1.4: amidase

This is an abbreviated version!
For detailed information about amidase, go to the full flat file.

Word Map on EC 3.5.1.4

Reaction

a monocarboxylic acid amide
+
H2O
=
a monocarboxylate
 +
NH3

Synonyms

4-guanidinobutyramide hydrolase, A-amidase, acetamidase, acid transferase, acylamidase, acylase, AMI1, amidase, amidase 1, amide hydrolase, amide transferase, amidohydrolase, AmiE, Ana, anandamide hydrolase, AtFAAH, Azl13, C-amidase, deaminase, ester transferase, FAAH, FAAH-1, FAAH-2, fatty acid amide hydrolase, fatty acid amide hydrolase 1, fatty acylamidase, half-amidase, indole-3-acetamide amidohydrolase, K1, mHG, Mhpg, More, murein peptide amidase A, mycothiol-S-conjugate amidase, N-acetylaminohydrolase, N-acylethanolamine acid amidase, N-acylethanolamine-hydrolyzing acid amidase, N-acylethanolaminehydrolyzing acid amidase, NAAA, NAE-hydrolyzing acid amidase, PamH, PYCH_10400, R-stereospecific amidase, RhAmidase, signature amidase, SsAH, SSAM, SSO2122, tissue kallikrein, Wide spectrum amidase

ECTree

     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.1 In linear amides
                3.5.1.4 amidase

Engineering

Engineering on EC 3.5.1.4 - amidase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C145A
-
mutant enzyme shows 9.7% of wild-type eactivity
C145S
-
mutant enzyme shows 6.2% of wild-type eactivity
D133A
-
inactive mutant enzyme
D133E
-
mutant enzyme shows 0.16% of wild-type eactivity
K36A
-
inactive mutant enzyme
K36R
-
mutant enzyme shows 9.5% of wild-type eactivity
S113A
-
inactive mutant enzyme
S113T
-
inactive mutant enzyme
S114A
-
inactive mutant enzyme
S114T
-
mutant enzyme shows 0.26% of wild-type eactivity
S137A
-
mutant enzyme shows 0.59% of wild-type eactivity
S137T
-
inactive mutant enzyme
S214T
-
mutant enzyme shows 83% of wild-type eactivity
C118A
complete loss of activity
K84A
9% decrease in activity compared to wild-type
Q11A
20% decrease in activity compared to wild-type
K84A
site-directed mutagenesis, the mutant shows no detectable hydrolysis activity
S159A
site-directed mutagenesis, the mutant shows no detectable hydrolysis activity
S183A
site-directed mutagenesis, the mutant shows no detectable hydrolysis activity
C166A
-
mutant catalytically inactive
C166S
-
mutant catalytically inactive
E59D
inactive mutant
E59Q
inactive mutant
E59V
-
mutant catalytically inactive
K134B
inactive mutant
K134R
200fold reduction in activity compared to wild type enzyme
T103I
T103I-W138G
-
mutant with increased instability and less themrmostable
W138G
-
mutant able to use acetanilide as a carbon source
T103I
-
site-directed mutagenesis, binding of specific monoclonal antibodies to the mutant enzyme compared to the wild-type enzyme
-
C249A
-
inhibition of the mutant by ibuprofen is similar than that of wild type
S152A
-
inhibition of the mutant by ibuprofen is similar than that of wild type
S218A
-
inactive mutant
S195A
catalytically inactive mutant
D487N
-
site-specific mutagenesis, the D487N mutation is located in the center of the protein, far distant from the 33-48 segment. The mutant amidase, like the wild-type enzyme, responds to changes in pH and temperature with a conformational change affecting the dimer-octamer equilibrium
K96R
retains the ability to hydrolyse amides but hydrolyses nitriles more efficiently than the wild-type enzyme
L34P
-
site-specific mutagenesis, the mutant amidase, in contrast to the wild-type enzyme, is unaffected by pH and temperature remaining always in the dimeric state
T319I
-
site-specific mutagenesis, the T319I mutation is located in a strand on the surface of the protein, which is far from, and opposite to, the N-terminal segment. The mutant amidase, like the wild-type enzyme, responds to changes in pH and temperature with a conformational change affecting the dimer-octamer equilibrium
K96R
-
retains the ability to hydrolyse amides but hydrolyses nitriles more efficiently than the wild-type enzyme
-
Y41C
-
no structural modifications in the Y41C mutant, the pH-spectrum is slightly increased
-
C141A
site-directed mutagenesis, inactive mutant
E41A
site-directed mutagenesis, inactive mutant
K107A
site-directed mutagenesis, inactive mutant
E41A
-
site-directed mutagenesis, inactive mutant
-
K107A
-
site-directed mutagenesis, inactive mutant
-
additional information